Biology Experiment 4: Enzyme Activity

A biological catalyst that speeds up chemical reactions in living organisms without being consumed in the process.

Each enzyme typically acts on a specific substrate or type of substrate, ensuring reactions are precisely controlled.

The specific region on an enzyme where a substrate binds and the chemical reaction occurs.

The molecule or molecules that an enzyme acts upon.

The temporary complex formed when a substrate binds to an enzyme's active site.

The initial energy required for a reaction to proceed.

The amount of substrate available to bind with enzyme molecules.

The amount of enzyme available to catalyze reactions.

A point where all enzyme active sites are occupied, and adding more substrate does not increase the reaction rate.

Increasing enzyme concentration increases the reaction rate if substrate is plentiful, as more active sites are available.

The temperature at which an enzyme functions best, usually around organism bodily temperature.

If the temperature is too high, enzymes lose their shape and functionality (denature) due to disruption in bonds holding the enzyme's structure together.

Each enzyme has a pH level where it performs best; this varies by enzyme.

Excessive deviations from the enzyme's optimal pH disrupts bonds within the enzyme, altering its shape, specifically the active site.

Increasing substrate concentration increases reaction rate until saturation point is reached, because more substrate molecules can collide with enzyme molecules.

Catalase breaks down hydrogen peroxide into water and oxygen.

The point where all enzyme active sites are occupied, and adding more substrate will not increase the reaction rate.

The reaction rate increases because more substrate molecules collide with enzyme molecules.

The reaction rate increases if there's excess substrate, as more active sites become available for the substrate molecules to bind to.

Changes in pH can disrupt bonds within the enzyme, altering its shape and active site, potentially hindering its function.

Enzymes are biological catalysts that speed up chemical reactions in living organisms without being consumed in the process. They are crucial for maintaining life, as they regulate virtually every biochemical reaction that occurs in cells.

Enzymes are primarily proteins. However, there are some RNA-based enzymes called ribozymes.

Enzymes work by lowering the activation energy of a reaction. This is the initial energy required for a reaction to proceed. By reducing this energy, enzymes make it easier and faster for reactions to happen.

Enzyme activity is influenced by several factors that can affect the rate at which enzymes catalyze reactions. These factors include substrate concentration, enzyme concentration, temperature, pH, presence of cofactors and coenzymes, and presence of inhibitors or activators.

Increasing enzyme concentration increases the reaction rate if there is a plentiful supply of substrate. This is because more active sites become available.

If the temperature is too high, enzymes lose their shape and functionality (denature) due to disruption in the bonds holding the enzyme's structure together.

Each enzyme has a pH level where it performs best. This varies by enzyme.

When substrate concentration is low, the reaction rate is low because there are fewer substrate molecules available to bind with enzyme molecules.

Enzymes are biological catalysts that speed up chemical reactions without being consumed in the process.

Enzymes are primarily proteins, folded into complex 3D shapes.

Enzymes work by lowering the activation energy required for a reaction to start.

Each enzyme works best at a specific temperature, often around the body temperature of the organism.

Each enzyme has a specific pH range where it operates best.

The reaction rate increases as more substrate molecules collide with enzyme molecules, leading to more frequent reactions. However, this trend only applies until all active sites are occupied.

Increasing the concentration of enzymes increases the reaction rate, provided there's enough substrate. This is because more active sites become available for substrate binding.

Changes in pH can disrupt the enzyme's shape, particularly affecting the active site, potentially hindering its function.

Catalase breaks down hydrogen peroxide, a potentially harmful byproduct of metabolism, into harmless water and oxygen.